Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2001-4-16
pubmed:abstractText
The two previously reported human glutathione S-transferase isozymes, hGST5.8 and hGSTA4-4, have been suggested to be similar because of their comparable activities toward 4-hydroxynonenal-GSH conjugation. Here, we demonstrate that hGST5.8 and hGSTA4-4 are distinct. Antibodies raised against hGSTA4-4 did not recognize hGST5.8, and antibodies raised against mouse GSTA4-4 that cross-react with hGST5.8 did not recognize hGSTA4-4. The pI value of hGSTA4-4 was found to be 8.4, as opposed to the pI value of 5.8 for hGST5.8. The two isozymes are differentially expressed in human tissues and there are significant differences in their kinetic properties. While both isozymes showed a strong expression in liver and testis, hGSTA4-4 was not detected in brain where hGST5.8 was present. In the pancreas, a strong expression of hGST5.8 was observed while hGSTA4-4 was barely detectable in this tissue.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-291X
pubmed:author
pubmed:copyrightInfo
Copyright 2001 Academic Press.
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
282
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1268-74
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Two distinct 4-hydroxynonenal metabolizing glutathione S-transferase isozymes are differentially expressed in human tissues.
pubmed:affiliation
Department of Human Biological Chemistry and Genetics, UTMB, Galveston, Texas 77555-1067, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.